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Protein

Vacuolar-sorting protein SNF7

Gene

SNF7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB). Acts a component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruitment of late-acting components of the sorting machinery. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complex assemblies. Appears to sequester MVB cargo. Recruits BRO1, which in turn recruits DOA4, which deubiquitinates cargos before their enclosure within MVB vesicles.2 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct

GO - Biological processi

  • cellular response to anoxia Source: SGD
  • intralumenal vesicle formation Source: SGD
  • late endosome to vacuole transport Source: SGD
  • protein transport Source: UniProtKB-KW
  • ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Source: SGD
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-32186-MONOMER.
ReactomeiREACT_303262. Endosomal Sorting Complex Required For Transport (ESCRT).

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar-sorting protein SNF7
Alternative name(s):
DOA4-independent degradation protein 1
Vacuolar protein-sorting-associated protein 32
Gene namesi
Name:SNF7
Synonyms:DID1, VPS32
Ordered Locus Names:YLR025W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XII

Organism-specific databases

CYGDiYLR025w.
EuPathDBiFungiDB:YLR025W.
SGDiS000004015. SNF7.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • ESCRT III complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 240240Vacuolar-sorting protein SNF7PRO_0000211446Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei72 – 721Phosphothreonine2 Publications
Modified residuei119 – 1191Phosphoserine1 Publication
Modified residuei193 – 1931Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP39929.
PaxDbiP39929.
PeptideAtlasiP39929.

Expressioni

Gene expression databases

GenevestigatoriP39929.

Interactioni

Subunit structurei

Self-associates. Core component of the ESCRT-III complex (endosomal sorting required for transport complex III). ESCRT-III appears to be sequentially assembled as a flat lattice on the endosome membrane and forms a transient 450 kDa complex that contains DID4, oligomerized SNF7, VPS20 and VPS24. SNF7 oligomerization into a membrane-associated filament is nucleated by association of SNF7 with VPS20; the process is terminated through association of VPS24, possibly by capping the SNF7 filament. VPS24 subsequently associates with DID4/VPS2. Interacts with VTA1; the interaction requires DID2. Interacts with BRO1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself7EBI-17554,EBI-17554
BRO1P485823EBI-17554,EBI-3768
DID4P361084EBI-17554,EBI-26574
HEH2Q032813EBI-17554,EBI-22131
VPS20Q042724EBI-17554,EBI-28157
VPS4P529174EBI-17554,EBI-20475

Protein-protein interaction databases

BioGridi31299. 108 interactions.
DIPiDIP-1747N.
IntActiP39929. 28 interactions.
MINTiMINT-389266.
STRINGi4932.YLR025W.

Structurei

3D structure databases

ProteinModelPortaliP39929.
SMRiP39929. Positions 20-95, 121-175.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi68 – 714Poly-Lys
Compositional biasi216 – 22813Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the SNF7 family.Curated

Phylogenomic databases

eggNOGiNOG291419.
GeneTreeiENSGT00390000005006.
HOGENOMiHOG000209960.
InParanoidiP39929.
KOiK12194.
OMAiENEARIF.
OrthoDBiEOG72RN9W.

Family and domain databases

InterProiIPR005024. Snf7_fam.
[Graphical view]
PfamiPF03357. Snf7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39929-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWSSLFGWTS SNAKNKESPT KAIVRLREHI NLLSKKQSHL RTQITNQENE
60 70 80 90 100
ARIFLTKGNK VMAKNALKKK KTIEQLLSKV EGTMESMEQQ LFSIESANLN
110 120 130 140 150
LETMRAMQEG AKAMKTIHSG LDIDKVDETM DEIREQVELG DEISDAISRP
160 170 180 190 200
LITGANEVDE DELDEELDML AQENANQETS KIVNNNVNAA PISENKVSLP
210 220 230 240
SVPSNKIKQS ENSVKDGEEE EDEEDEDEKA LRELQAEMGL
Length:240
Mass (Da):26,987
Last modified:February 1, 1995 - v1
Checksum:i5241A18BB181F0C1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti173 – 1731E → G in AAS56528 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09751 Genomic DNA. No translation available.
Z73197 Genomic DNA. Translation: CAA97548.1.
AY558202 Genomic DNA. Translation: AAS56528.1.
BK006945 Genomic DNA. Translation: DAA09343.1.
PIRiS52590.
RefSeqiNP_013125.1. NM_001181912.1.

Genome annotation databases

EnsemblFungiiYLR025W; YLR025W; YLR025W.
GeneIDi850712.
KEGGisce:YLR025W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09751 Genomic DNA. No translation available.
Z73197 Genomic DNA. Translation: CAA97548.1.
AY558202 Genomic DNA. Translation: AAS56528.1.
BK006945 Genomic DNA. Translation: DAA09343.1.
PIRiS52590.
RefSeqiNP_013125.1. NM_001181912.1.

3D structure databases

ProteinModelPortaliP39929.
SMRiP39929. Positions 20-95, 121-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31299. 108 interactions.
DIPiDIP-1747N.
IntActiP39929. 28 interactions.
MINTiMINT-389266.
STRINGi4932.YLR025W.

Proteomic databases

MaxQBiP39929.
PaxDbiP39929.
PeptideAtlasiP39929.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR025W; YLR025W; YLR025W.
GeneIDi850712.
KEGGisce:YLR025W.

Organism-specific databases

CYGDiYLR025w.
EuPathDBiFungiDB:YLR025W.
SGDiS000004015. SNF7.

Phylogenomic databases

eggNOGiNOG291419.
GeneTreeiENSGT00390000005006.
HOGENOMiHOG000209960.
InParanoidiP39929.
KOiK12194.
OMAiENEARIF.
OrthoDBiEOG72RN9W.

Enzyme and pathway databases

BioCyciYEAST:G3O-32186-MONOMER.
ReactomeiREACT_303262. Endosomal Sorting Complex Required For Transport (ESCRT).

Miscellaneous databases

NextBioi966772.
PROiP39929.

Gene expression databases

GenevestigatoriP39929.

Family and domain databases

InterProiIPR005024. Snf7_fam.
[Graphical view]
PfamiPF03357. Snf7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular and genetic analysis of the SNF7 gene in Saccharomyces cerevisiae."
    Tu J., Vallier L.G., Carlson M.
    Genetics 135:17-23(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins."
    Howard T.L., Stauffer D.R., Degnin C.R., Hollenberg S.M.
    J. Cell Sci. 114:2395-2404(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting."
    Babst M., Katzmann D.J., Estepa-Sabal E.J., Meerloo T., Emr S.D.
    Dev. Cell 3:271-282(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE ESCRT-III COMPLEX, INTERACTION WITH VPS20, SUBCELLULAR LOCATION.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces cerevisiae."
    Bowers K., Lottridge J., Helliwell S.B., Goldthwaite L.M., Luzio J.P., Stevens T.H.
    Traffic 5:194-210(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BRO1.
  9. "Structural basis for endosomal targeting by the Bro1 domain."
    Kim J., Sitaraman S., Hierro A., Beach B.M., Odorizzi G., Hurley J.H.
    Dev. Cell 8:937-947(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BRO1.
  10. "Vta1p and Vps46p regulate the membrane association and ATPase activity of Vps4p at the yeast multivesicular body."
    Lottridge J.M., Flannery A.R., Vincelli J.L., Stevens T.H.
    Proc. Natl. Acad. Sci. U.S.A. 103:6202-6207(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VTA1.
  11. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  12. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Ordered assembly of the ESCRT-III complex on endosomes is required to sequester cargo during MVB formation."
    Teis D., Saksena S., Emr S.D.
    Dev. Cell 15:578-589(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSEMBLY OF THE ESCRT-III COMPLEX.
  14. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSNF7_YEAST
AccessioniPrimary (citable) accession number: P39929
Secondary accession number(s): D6VY27, E9P8V6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 27, 2015
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3270 molecules/cell in log phase SD medium.1 Publication

Caution

Was originally thought to be a nuclear protein and mutations were shown to prevent full derepression of the SUC2 (invertase) gene.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.